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The cooperation of B-Myb with the coactivator p300 is orchestrated by cyclins A and D1.

Authors
  • Schubert, Stephan
  • Horstmann, Sebastian
  • Bartusel, Thorsten
  • Klempnauer, Karl-Heinz
Type
Published Article
Journal
Oncogene
Publisher
Springer Nature
Publication Date
Feb 19, 2004
Volume
23
Issue
7
Pages
1392–1404
Identifiers
PMID: 14973551
Source
Medline
License
Unknown

Abstract

B-Myb is a highly conserved member of the Myb family of transcription factors whose activity is regulated during the cell cycle. Previous work has shown that the activity of B-Myb is stimulated by cyclin A/Cdk2-dependent phosphorylation whereas interaction of B-Myb with cyclin D1 inhibits its activity. Here, we have investigated the role of p300 as a coactivator for B-Myb. We show that B-Myb-dependent transactivation is stimulated by p300 as a result of interaction between B-Myb and p300. We have mapped the sequences responsible for the interaction of B-Myb and p300 to the E1A-binding region of p300 and the transactivation domain of B-Myb, respectively. Furthermore, our data suggest that phosphorylation of B-Myb stimulates its acetylation by p300 and that the acetylation of B-Myb is necessary for the full stimulation of its transactivation potential by p300. We have also studied the effect of cyclin D1 on the cooperation of B-Myb and p300. Based on our results we propose that cyclin D1 inhibits the activity of B-Myb by interfering with the interaction of B-Myb and p300. The data reported here provide novel insight into the mechanisms by which the activity of B-Myb is regulated during the cell cycle. Taken together they suggest that the coactivator p300 plays an important role in this regulation and that the cooperation of B-Myb and p300 is orchestrated by cyclins A and D1.

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